ID A0A1D3THR0_9APIC Unreviewed; 488 AA.
AC A0A1D3THR0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Vivapain-3, putative {ECO:0000313|EMBL:SCP04481.1};
GN Name=PocGH01_09021600 {ECO:0000313|EMBL:SCP04481.1};
GN ORFNames=POCGH01_09021600 {ECO:0000313|EMBL:SCP04481.1};
OS Plasmodium ovale (malaria parasite P. ovale).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=36330 {ECO:0000313|EMBL:SCP04481.1, ECO:0000313|Proteomes:UP000242942};
RN [1] {ECO:0000313|EMBL:SCP04481.1, ECO:0000313|Proteomes:UP000242942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PocGH01 {ECO:0000313|EMBL:SCP04481.1};
RG Pathogen Informatics;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; LT594590; SCP04481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3THR0; -.
DR SMR; A0A1D3THR0; -.
DR VEuPathDB; PlasmoDB:PocGH01_09021600; -.
DR VEuPathDB; PlasmoDB:POWCR01_090016900; -.
DR Proteomes; UP000242942; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 1.10.287.2250; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF1017; CLAN CA, FAMILY C1, CATHEPSIN L OR K-LIKE CYSTEINE PEPTIDASE; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242942};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 169..225
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 270..480
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 488 AA; 56839 MW; 58FC4AF6321F81B7 CRC64;
MDYHMQYFSN ESTKGEMEVF VERENDNNKM FFKKKKNLLI IVYVSAFCAI AYSIIYFSKS
SKKNNVFTDS SEDIVTDDYI ISSLLKSKNG KKYIVSKIEE LISFYDKNSD FEKGEESNKV
VKTNACKDNR CVTINRNNSE DLRTEKKNYD VNFFDTKFLM RNLESVNAFY IFMKEHGKKY
TSVDEMEKKF IAFSKNIAKI DAHNKSNSLY KKGVNRFSDL SFEEFQKKYL TLKEFDLKKT
TLNKSRSSDY EDIIIKYKTD DRKFDYIKHD WRELNGVTPI RDQLNCGSCW AFSTVGVVES
QYAIRRKQML SLSEQELVDC SFQNYGCDGG LIVFAFDDMI DLGGLCTAEE YPYVDLKPEL
CDIYKCKNKY EIKTYAEIPQ VRFKEAISFL GPISVSINAT DDFAYYKNGI FDGSCSYIAN
HAVILVGYGM EEIYNNQTKQ NEKQYYYIIK NSWGEQWGEK GFMRIKTDEF GLEKTCSLGA
QAFIALIE
//